ArticleThe Journal of antibiotics2026
P450 cyptide synthase KwwB catalyzes non-native cross-link at Tyr-C3-Trp-N1 and tolerates leader peptide mutations.
Article in The Journal of antibiotics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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8 authors.
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Abstract
Cyptides refer to a rapidly growing class of ribosomally synthesized and post-translationally modified peptides (RiPPs) containing biaryl cyclophanes installed by P450 enzymes. Here, we further investigated P450 cyptide synthase KwwB from Kitasatospora sp. GAS204B, which expands the KwwB-catalyzed chemical repertoire to non-native cross-link between Tyr-C3 and Trp-N1 at the YxW motif. In addition, we demonstrated that KwwB tolerates leader peptide mutations at positions -11 through -2, with the exception of position -4, which contains a conserved Pro residue. This result provides an additional toolkit for cross-linked peptide modification.
Identifiers
42806039What OpenQuestion holds
Registered trials
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